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Human osteosarcoma derived clonal variants: stable differences in cell surface composition.

D De Martelaere·J J Cassiman·F Van Leuven·J Verlinden·P Marynen·J Casteleyn·H Van den Berghe
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AminopeptidasesCD13 AntigensCell LineCell MembraneClone CellsFibronectinsGenetic VariationHumansLow Density Lipoprotein Receptor-Related Protein-1OsteosarcomaReceptors, ImmunologicSurface Propertiesgamma-GlutamyltransferaseComparative StudyJournal ArticleResearch Support, Non-U.S. Gov't

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D De Martelaere, J J Cassiman, F Van Leuven, J Verlinden, P Marynen, J Casteleyn, H Van den Berghe. 1982. Human osteosarcoma derived clonal variants: stable differences in cell surface composition.. https://doi.org/10.1016/0309-1651(82)90120-5

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PubMed2024

Polymorphic positions 349 and 725 of the autoimmunity-protective allotype 10 of ER aminopeptidase 1 are key in determining its unique enzymatic properties.

INTRODUCTION: ER aminopeptidase 1 (ERAP1) is a polymorphic intracellular aminopeptidase with key roles in antigen presentation and adaptive immune responses. ERAP1 allotype 10 is highly protective toward developing some forms of autoimmunity and displays unusual functional properties, including very low activity versus some substrates. METHODS: To understand the molecular mechanisms that underlie the biology of allotype 10, we studied its enzymatic and biophysical properties focusing on its unique polymorphisms V349M and Q725R. RESULTS: Compared to ancestral allotype 1, allotype 10 is much less effective in trimming small substrates but presents allosteric kinetics that ameliorate activity differences at high substrate concentrations. Furthermore, it is inhibited by a transition-state analogue via a non-competitive mechanism and is much less responsive to an allosteric small-molecule modulator. It also presents opposite enthalpy, entropy, and heat capacity of activation compared to allotype 1, and its catalytic rate is highly dependent on viscosity. Polymorphisms V349M and Q725R significantly contribute to the lower enzymatic activity of allotype 10 for small substrates, especially at high substrate concentrations, influence the cooperation between the regulatory and active sites, and regulate viscosity dependence, likely by limiting product release. CONCLUSIONS: Overall, our results suggest that allotype 10 is not just an inactive variant of ERAP1 but rather carries distinct enzymatic properties that largely stem from changes at positions 349 and 725. These changes affect kinetic and thermodynamic parameters that likely control rate-limiting steps in the catalytic cycle, resulting in an enzyme optimized for sparing small substrates and contributing to the homeostasis of antigenic epitopes in the ER.

Aminopeptidases↗
PubMed2003

Aminopeptidases function as endocytic receptors in the trophotaenial placenta of the goodeid fish, Ameca splendens (Teleostei: Atheriniformes).

Viviparity in goodeid teleosts is characterized by the elaboration of trophotaeniae, extraembryonic proctodaeal appendages facilitating maternal-embryonic nutrient transfer. The trophotaenial absorptive cells (TACs) express aminopeptidases (APs) such as APA, APN, gamma-glutamyltransferase (gamma-GT), dipeptidyl aminopeptidase (DAP) IV, and neutral endopeptidase (NEP) as inferred from the results of cleavage experiments with, respectively, Glu-alpha-(4M beta NA), Ala-(4M beta NA), Glu-gamma-(4M beta NA), Gly-Pro-(4M beta NA), and Gl-(Ala)(3)-(4M beta NA). Enzyme reaction product was localized to the apical and basolateral plasma membrane as well as to some intracellular compartments. In the accompanying report (Schindler, 2003) evidence is presented that the trophotaeniae of Ameca splendens embryos randomly, yet specifically, bind and ingest proteins as well as certain copolymers of amino acids. Present results demonstrate that endocytosis is significantly inhibitable by unspecific proteinase inhibitors, such as diisopropylphosphorofluoride, phenylmethanesulfonylfluoride, antipain, 1.10-phenanthroline, and dithiothreitol. The specific microbial AP inhibitors amastatin, bestatin, and phosphoramidon suppressed protein binding to TACs more effectively when added in combination than did either agent alone. Moreover, in the presence of 4M beta NA assay substrates of APs the capability of TACs to bind proteins was significantly reduced. Conversely, the rate at which 4M beta NA substrates were cleaved by trophotaenial APs was modified in the presence of proteins. Depending on protein concentrations the AP-catalyzed reactions either decreased or increased in velocity. Analysis of the enzyme kinetics by methods of linear transformation suggests that proteins bind to APs competitively, thereby adopting the role of enzyme inhibitors. On the other hand, protein binding to APs appears to be a signal to translocate enzymes from an internal pool to the surface membrane. In the presence of primaquine, the rate of AP-catalyzed cleavage of 4M beta NA substrates was significantly reduced. That can be put down to the fact that weak bases disrupt the recycling of endocytosed membrane constituents. In conclusion, there is evidence that APs in the trophotaenial placenta of A. splendens function as scavenger receptors mediating in the delivery of embryotrophic proteins for lysosomal degradation.

Aminopeptidases↗
PubMed2003

Purification and properties of an arginyl aminopeptidase from Debaryomyces hansenii.

A metallo arginyl aminopeptidase (EC 3.4.11.6) activated by Co(2+) was isolated from Debaryomyces hansenii CECT 12487. The enzyme was purified after precipitation with protamine sulphate, followed by a weak anion exchange chromatography, gel filtration chromatography and a strong anion exchange chromatography. The arginyl aminopeptidase (AAP) was purified 337 folds, with a 18% recovery. The AAP appeared to be a dimer with a molecular mass of 101 kDa. The enzyme was active in the pH range from 6 to 9. The optimal activity was detected at pH 7.0 and at 37 degrees C. AAP activity was inhibited by typical aminopeptidase inhibitors (puromycin and bestatin), reducing agents (DTT), chelating agents (EDTA, EGTA and phenantroline) and sulphydryl groups reagents (iodoacetate). Ca(2+), Mn(2+) and Co(2+) activated the enzyme, while Cu(2+), Cd(2+), Hg(2+) and Mg(2+) inhibited it. The K(m) values calculated for Arg-AMC (7-amido-4-methylcoumarin) and Leu-AMC were 0.071 and 0.094 mM, respectively. The enzyme showed maximum specificity for basic amino acids (Arg and Lys), but was also able to hydrolyze non-charged amino acids (Leu, Met and Ala) and, at a minor rate, aromatic amino acids (Phe and Tyr). AAP showed higher activity when an acid residue was located at the C-terminal position of dipeptides. The described purification of an arginyl aminopeptidase from the yeast D. hansenii can contribute to the lack of knowledge about the exopeptidase activity in one of the yeasts more frequently isolated in sausage and to understand its role during the ripening of a fermented sausage.

Aminopeptidases↗